Abstract
The cyclization of polypeptides confers enhanced stability, specificity, binding affinity, and cell permeability, making it a common feature in the backbone structure of natural products. Disulfide bonds are widely found in active peptides and play a crucial role in maintaining their secondary structure. In this study, we present a sulfur exchange reaction-based method for constructing disulfide bonds using 2,2′-dithiobis(5-nitropyridine) as a mediator. This method exhibits excellent substrate adaptability and compatibility with conventional functional groups. It also demonstrates rapid reaction efficiency, allowing successful disulfide bond formation under various pH conditions. Moreover, the products and additives can be easily separated, showing the potential of this method for screening disulfide bond-rich peptides in future research.
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